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Highly functionalized terpyridines as competitive inhibitors of AKAP-PKA interactions

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Item Type:Article
Title:Highly functionalized terpyridines as competitive inhibitors of AKAP-PKA interactions
Creators Name:Schäfer, G. and Milić, J and Eldahshan, A and Götz, F. and Zühlke, K. and Schillinger, C. and Kreuchwig, A. and Elkins, J.M. and Abdul Azeez, K.R.A. and Oder, A. and Moutty, M.C. and Masada, N. and Beerbaum, M. and Schlegel, B. and Niquet, S. and Schmieder, P. and Krause, G. and von Kries, J.P. and Cooper, D.M.F. and Knapp, S. and Rademann, J. and Rosenthal, W. and Klussmann, E.
Abstract:A good fit: Interactions between A-kinase anchoring proteins (AKAPs) and protein kinase A (PKA) play key roles in a plethora of physiologically relevant processes whose dysregulation causes or is associated with diseases such as heart failure. Terpyridines have been developed as α-helix mimetics for the inhibition of such interactions and are the first biologically active, nonpeptidic compounds that block the AKAP binding site of PKA.
Keywords:AKAP, Peptide Mimetics, Protein Kinase A, Protein-Protein Interactions, Suzuki Coupling, Terpyridines
Source:Angewandte Chemie International Edition
Page Range:12187-12191
Date:11 November 2013
Official Publication:https://doi.org/10.1002/anie.201304686
PubMed:View item in PubMed

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